ABSTRACT
This chapter concentrates on a comparison of pressure and temperature effects on proteins. It considers thermodynamic as well as kinetic. The chapter analyzes the effect of pressure on egg yolk. It is well known from the preparation of a hard-boiled egg that the yolk becomes solid at a slightly higher temperature than the white. The study of the effects of pressure on proteins has received considerable attention in recent years. In general, low pressures induce reversible changes such as the dissociation of protein-protein complexes, the binding of ligands, and conformational changes. The biologically active structure of a protein is only stable within restricted conditions of temperature, pressure, and solvent composition. Outside this range, unfolding or denaturation takes place. When the protein concentration is sufficiently high, aggregation may take place followed by gel formation. Protein denaturation and gel formation induced by temperature and solvent conditions may be studied by several experimental approaches.
